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Genetically Encoded Lysine Residue-Selective photo-crosslinker to Capture and Identify Protein Interactions in Living Cells

Genetically Encoded Lysine Residue-Selective Photo-Crosslink...

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第十一届全国化学生物学学术会议

作者： Wei Hu Yi Yuan Cai-Hu Wang Hong-Tao Tian An-Di,Guo Hui-Jun Nie Hao Hu Minjia Tan Zhuo Tang Xiao-Hua Chen Chinese Academy of Sciences Key Laboratory of Receptor Research Shanghai Institute of Materia MedicaChinese Academy of Sciences

Protein-protein interactions(PPIs) play crucial roles in regulation of many biological *** genetically encoding photo-crosslinkers forming covalent linkage with any proximal residue is an attractive strategy for addressing the challenge of capturing weak and transient protein ***,such non-selective crosslinking increases background crosslinking,makes crosslinking sites unpredictable,generates excessive number of crosslinked peptides with variable residues,thus dramatically complicates mass spectrometric analysis(MS),and artificially leads to false positive interacting partners for ***,we developed a conceptually new approach that genetically encoded,residue-selective photo-crosslinker(o-NBAK) to capture PPIs in temporal controlled *** novel probe is efficient to capture PPIs upon UV light activation,providing lysine selective crosslinking sites and predictable crosslinked peptides,facilitating mass spectrometric analysis and mapping accurate interaction ***,this probe enables the capture of elusive enzyme-substrate interaction with directly interacting lysine and validation of acetylation site of the substrate,which could exclude false positive substrates for enzymes and directly provide the post-translation modification site of substrates,thus,enable specificity,accuracy and reliability for enzyme-substrate interactions .Combining advantages of temporal control and the unique ability of residue selectivity,this genetically encoded photo-crosslinkers will be a powerful tool for identification of dynamic,weak,and transient protein interactions in living cells with specificity,accuracy,and reliability,thus,for better understanding of biological processes and pathophysiology.

关键词： photo-crosslinker PPIs residue-selective probe o-NBAK

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An Active Based Multifunctional Probe for Off-On Fluorescent Detection,Labeling and Profiling of Protein Sulfenic Acid in Cells

An Active Based Multifunctional Probe for Off-On Fluorescent...

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第十一届全国化学生物学学术会议

作者： Man Li Chunrong Liu Key Laboratory of Pesticide and Chemical Biology Ministry of EducationSchool of ChemistryCentral China Normal University

As a significant post-translational modification, protein S-sulfenylation triggered by reactive oxygen species（ROS） could modulate the protein functions, redox homeostasis, various signaling pathways and cellular functions, and is also associated with many diseases. Thus, protein S-sulfenylation is thought as the center of redox biologies and pathologies.[1] However, the dynamic nature of protein S-sulfenylation, transient fate of protein sulfenic acids and the lack of probes which enable the spatial and temporal profiling of intracellular protein S-sulfenylation have hindered our understanding of such redox PTM. Herein we report an active based multifunctional probe（SA-HYD） which enables "off-on" fluorescent detection, labeling and profiling of protein S-sulfenylation within cells. We proved that SA-HYD was capable of not only tracking the intracellular protein S-sulfenylation spatially and temporally, but also capturing and identifying the S-sulfenylated proteins in complex cellular environments. Besides, SA-HYD has been applied successfully in studying the kinetics of protein S-sulfenylation in both physiological buffer and cell lysates. Therefore, we deem that this ABPP probe could provide a robust tool for better understanding the physiological and pathological roles of protein S-sulfenylation.

关键词： redox biology protein S-sulfenylation activity-based protein profiling probe naphthylhydrazine photo-crosslinker

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